A novel serine alkaline protease from Bacillus altitudinis GVC11 and its application as a dehairing agent
A novel serine alkaline protease from Bacillus altitudinis GVC11 and its application as a dehairing agent
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DOI：
10.1007/s00449-010-0483-x
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发表时间：
2011-05-01
影响因子：
3.8
通讯作者：
Reddy, Gopal
中科院分区：
文献类型：
--
作者：
Kumar, E. Vijay;Srijana, M.;Reddy, Gopal
对新分离的嗜碱性芽孢杆菌 GVC11 中的丝氨酸碱性蛋白酶进行了纯化和表征。通过丙酮沉淀、DEAE-纤维素阴离子交换层析将酶纯化至均质，比活性增加7.03倍，回收率15.25%。通过 SDS PAGE 估计碱性蛋白酶的分子量为 28 kDa，并通过酶谱分析进一步评估活性。该酶在 pH 8.5 至 12.5 的较宽范围内具有高活性，最适 pH 为 9.5。纯化酶的最适温度为45℃，Ca2+进一步提高了酶的热稳定性。 Ca2+和Mg2+增强酶活性，Hg2+抑制酶活性。本研究是第一份检查和描述高原芽孢杆菌产生高碱性蛋白酶的报告，以及其在 18 小时内对山羊皮的显着脱毛能力，而不干扰胶原蛋白和毛发完整性。
A serine alkaline protease from a newly isolated alkaliphilic Bacillus altitudinis GVC11 was purified and characterized. The enzyme was purified to homogeneity by acetone precipitation, DEAE-cellulose anion exchange chromatography with 7.03-fold increase in specific activity and 15.25% recovery. The molecular weight of alkaline protease was estimated to be 28 kDa by SDS PAGE and activity was further assessed by zymogram analysis. The enzyme was highly active over a wide range of pH 8.5 to 12.5 with an optimum pH of 9.5. The optimum temperature of purified enzyme was 45 A degrees C and Ca2+ further increased the thermal stability of the enzyme. The enzyme activity was enhanced by Ca2+ and Mg2+ and inhibited by Hg2+. The present study is the first report to examine and describe production of highly alkaline protease from Bacillus altitudinis and also its remarkable dehairing ability of goat hide in 18 h without disturbing the collagen and hair integrity.